Abstract

A viral tRNA-like structure has evolved a unique strategy to undergo a tertiary structure conformational switch that may help regulate viral regulation.

Highlights

  • The finding that non-coding RNAs are abundant and critical players in gene expression and regulation is one of the most significant discoveries in modern molecular biology [1]

  • turnip yellow mosaic virus (TYMV) is a positive-sense RNA virus that contains a single-stranded RNA genome, which acts both as the mRNA template for viral protein translation by cellular host ribosomes and as the RNA template for virus replication by a viral RNA-dependent RNA polymerase (RDRP)

  • The tRNAlike structure (TLS) secondary structure determined using nuclease probing data [7] subsequently revealed how the TLS achieved a tRNA-like fold and highlighted some important differences from canonical tRNA at the acceptor stem, which is the site of aminoacylation [7]

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Summary

Introduction

The finding that non-coding RNAs (ncRNAs) are abundant and critical players in gene expression and regulation is one of the most significant discoveries in modern molecular biology [1]. The bound elongation factor proteins are in turn thought to deliver TLS to the host ribosomal A-site, where the 5’ end of the viral genome can loop around to bind as an mRNA template. The terminal 3’-CCA sequence element of the TLS acts as a promoter for negative-strand synthesis during replication, but only when the TLS in not aminoacylated or bound to elongation factors [5,6].

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